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Direct inhibition of the yeast cyclin-dependent kinase Cdc28-Cln by Far1.

Science (New York, N.Y.) | Aug 26, 1994

http://www.ncbi.nlm.nih.gov/pubmed/8066461

Cell cycle arrest of Saccharomyces cerevisiae in G1 by the antimitogen alpha-factor is mediated by activation of a signal transduction pathway that results in inhibition of the cyclin-dependent kinase Cdc28-Cln. The Far1 protein is required for cell cycle arrest and associates with the Cdc28-Cln complex. The kinase activity of Cdc28-Cln was directly inhibited by Far1 both in vivo and in vitro, thus demonstrating that Far1 acts at the final step in the alpha-factor response pathway by inhibiting a G1 cyclin-dependent kinase.

Pubmed ID: 8066461 RIS Download

Mesh terms: CDC28 Protein Kinase, S cerevisiae | Cell Cycle Proteins | Cyclin-Dependent Kinase Inhibitor Proteins | Cyclins | Fungal Proteins | G1 Phase | Peptides | Phosphorylation | Protamine Kinase | Recombinant Fusion Proteins | Repressor Proteins | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins

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Associated grants

  • Agency: NIGMS NIH HHS, Id: GM31286

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